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Q03E83

- PUR9_PEDPA

UniProt

Q03E83 - PUR9_PEDPA

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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Pediococcus pentosaceus (strain ATCC 25745 / 183-1w)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

Functioni

Catalytic activityi

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: UniProtKB-HAMAP
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciPPEN278197:GI4Y-1458-MONOMER.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurHUniRule annotation
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferaseUniRule annotation (EC:2.1.2.3UniRule annotation)
Alternative name(s):
AICAR transformylaseUniRule annotation
IMP cyclohydrolaseUniRule annotation (EC:3.5.4.10UniRule annotation)
Alternative name(s):
ATICUniRule annotation
IMP synthaseUniRule annotation
InosinicaseUniRule annotation
Gene namesi
Name:purHUniRule annotation
Ordered Locus Names:PEPE_1458
OrganismiPediococcus pentosaceus (strain ATCC 25745 / 183-1w)
Taxonomic identifieri278197 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaePediococcus
ProteomesiUP000000773: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 511511Bifunctional purine biosynthesis protein PurHPRO_1000018922Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi278197.PEPE_1458.

Structurei

3D structure databases

ProteinModelPortaliQ03E83.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region.UniRule annotation

Sequence similaritiesi

Belongs to the PurH family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiGIGQADN.
OrthoDBiEOG6QCDFF.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

Q03E83-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKTALLSVSD KTGIVEFARG LVKADFRIIS TGGTKKVLEE AGLSIVSVEA
60 70 80 90 100
ITNFPEMLDG RVKTLHPAIH GGLLARRDLP EHLAALKEHN IDLIDLVCVN
110 120 130 140 150
LYPFKSTIMQ NGVTEAEAIE QIDIGGPSML RSAAKNFASV LPVVDPKDYQ
160 170 180 190 200
PVLAALAHQT DNVKFRRALA LKVFQHTAAY DTLIAQYLGQ NGEIFPDELT
210 220 230 240 250
KTYTKKQVMR YGENSHQKAA FYEDALPVPF SIAQAQQLHG KELSYNNIKD
260 270 280 290 300
ADAALKMSAE FNQPAVVAVK HMNPCGIGLG QNIEEAWDRA YEADSMSIFG
310 320 330 340 350
GIIVLNRPVD LATAEKMHKL FLEIIIAPSF EKEAFTVLAQ KKNLRIMTVD
360 370 380 390 400
FNQHQDAKEL ETVSVMGGLL VQEQDAVVET ATDFKVVSKR QPTESELKAM
410 420 430 440 450
VFGQTVVKHV KSNAIVITTD QQTLGIGAGQ MNRIGSVEIA VKQAEGSANF
460 470 480 490 500
KNAVMASDAF FPMEDCVEYA AKHGIKAIVE PGGSIKDQAS IDKADELGIS
510
LIFSGRRHFR H
Length:511
Mass (Da):55,930
Last modified:November 14, 2006 - v1
Checksum:iB4020CBDB5383A91
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000422 Genomic DNA. Translation: ABJ68489.1.
RefSeqiWP_011673675.1. NC_008525.1.
YP_804931.1. NC_008525.1.

Genome annotation databases

EnsemblBacteriaiABJ68489; ABJ68489; PEPE_1458.
GeneIDi4417281.
KEGGippe:PEPE_1458.
PATRICi22876226. VBIPedPen34213_1375.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CP000422 Genomic DNA. Translation: ABJ68489.1 .
RefSeqi WP_011673675.1. NC_008525.1.
YP_804931.1. NC_008525.1.

3D structure databases

ProteinModelPortali Q03E83.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 278197.PEPE_1458.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABJ68489 ; ABJ68489 ; PEPE_1458 .
GeneIDi 4417281.
KEGGi ppe:PEPE_1458.
PATRICi 22876226. VBIPedPen34213_1375.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230373.
KOi K00602.
OMAi GIGQADN.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci PPEN278197:GI4Y-1458-MONOMER.

Family and domain databases

Gene3Di 3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPi MF_00139. PurH.
InterProi IPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view ]
PANTHERi PTHR11692. PTHR11692. 1 hit.
Pfami PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR00355. purH. 1 hit.
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 25745 / 183-1w.

Entry informationi

Entry nameiPUR9_PEDPA
AccessioniPrimary (citable) accession number: Q03E83
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: October 29, 2014
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3